Structural comparison of two esterases from Drosophila mojavensis isolated by immunoaffinity chromatography

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Structural comparison of two esterases from Drosophila mojavensis isolated by immunoaffinity chromatography.

Antibodies raised against esterase-4 and esterase-5 from Drosophila mojavensis were coupled to Protein A-Sepharose CL-4B to prepare high-efficiency immunomatrices used for their purification. Final purification was achieved by anion-exchange h.p.l.c., in the case of esterase-5 followed by gel-filtration h.p.l.c. The resultant esterase preparations were homogeneous, as judged by gel-filtration h...

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The purification of chitin deacetylase from Mucor rouxii to homogeneity employing conventional methods has already been described. However, a lengthy protocol is required resulting in a low yield and specific activity for the enzyme . A 169-fold one-step purification of chitin deacetylase by immunoaffinity chromatography is reported, resulting in a homogeneous enzyme preparation. The enzyme pur...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1986

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2380691